BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17744

Title: 3D ssNMR structure of membrane embedded KcsA-Kv1.3 channel (Inactivated state)   PubMed: 23882077

Authors: Nand, D.; Ader, C.; Prokofyev, A.; Hornig, S.; A Bonvin, M.; Killian, A.; Becker, S.; Pongs, O.; Baldus, M.

Citation: van der Cruijsen, Elwin; Nand, Deepak; Weingarth, Markus; Prokofyev, Alexander; Hornig, Sonke; Cukkemane, Abhishek Arun; Bonvin, Alexandre M J J; Becker, Stefan; Hulse, Raymond; Perozo, Eduardo; Pongs, Olaf; Baldus, Marc. "Importance of lipid-pore loop interface for potassium channel structure and function."  Proc. Natl. Acad. Sci. U.S.A. 110, 13008-13013 (2013).

Assembly members:
KcsA-Kv1.3_(Inactivated_state), polymer, 94 residues, 9775.335 Da.

Natural source:   Common Name: Streptomyces lividans   Taxonomy ID: 1916   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces lividans

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
KcsA-Kv1.3_(Inactivated_state): SALHWRAAGAATVLLVIVLL AGSYLAVLAEADDPTSGFSS IPDALWWSVETATTVGYGDL YPVTLWGRCVAVVVMVAGIT SFGLVTAALATWFV

Data sets:
Data typeCount
13C chemical shifts250
15N chemical shifts39

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1KcsA-Kv1.3 (Inactivated state)1

Entities:

Entity 1, KcsA-Kv1.3 (Inactivated state) 94 residues - 9775.335 Da.

1   SERALALEUHISTRPARGALAALAGLYALA
2   ALATHRVALLEULEUVALILEVALLEULEU
3   ALAGLYSERTYRLEUALAVALLEUALAGLU
4   ALAASPASPPROTHRSERGLYPHESERSER
5   ILEPROASPALALEUTRPTRPSERVALGLU
6   THRALATHRTHRVALGLYTYRGLYASPLEU
7   TYRPROVALTHRLEUTRPGLYARGCYSVAL
8   ALAVALVALVALMETVALALAGLYILETHR
9   SERPHEGLYLEUVALTHRALAALALEUALA
10   THRTRPPHEVAL

Samples:

sample_1: KcsA-Kv1.3 (Inactivated state), [U-100% 13C; U-100% 15N], 5 mM; H2O 100%

sample_conditions_1: pH: 4.0; temperature: 243 K

Experiments:

NameSampleSample stateSample conditions
2D_13C-13C_CHHCsample_1solidsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17727